The protective action of ceruloplasmin on Fe2+ stimulated lysis of rat erythrocytes

• 1.1. Ceruloplasmin, a copper containing serum protein, was found to effectively protect washed rat erythrocytes against Fe²⁺ stimulated lysis.
• 2.2. It is proposed that Ceruloplasmin, through its Fe²⁺ oxidase activity, prevents the formation of superoxide radicals, known to cause hemolysis.

     

Ascorbate (vitamin c) and dehydroascorbate stimulation of copper induced hemolysis protective action of ceruloplasmin,albumin and apotransferrin

• 1.1. Copper ion induced lysis of rat erythrocytes was markedly stimulated by low concentrations of ascorbate and dehydroascorbate.
• 2.2. Ascorbate oxidase, superoxide dismutase, catalase or scavengers of hydroxyl radicals protected erythrocytes against copper-ascorbate stimulated lysis.
• 3.3. It is proposed that superoxide radicals and hydrogen peroxide cooperate in producing hydroxyl radicals, which are directly involved in hemolysis.
• 4.4. The serum proteins, ceruloplasmin. albumin and apotransferrin, also reduced the hemolytic action of copper-ascorbate, the order of effectiveness being; ceruloplasmin > albumin > apotransferrin.

     

Variation of l-gulonolactone oxidase activity in placental mammals

• 1.1. The activity of l-gulonolactone oxidase (EC 1.1.3.8) in livers of 49 species of eutherian mammals varied intraspecifically among individuals; coefficients of variation were 0.2 to 0.4 in many species.
• 2.2. Differences observed in l-gulonolactone oxidase activity among strains of laboratory rats and domestic rabbits are probably genetically controlled.
• 3.3. Pronounced sex differences in l-gulonolactone oxidase activity were found in some species, particularly in the genera Peromyscus, Reithrodontomys and Onychomys.
• 4.4. Mormota monax exhibited seasonal variation in l-gulonolactone oxidase somewhat like that previously observed in Sylvilagus floridanus; no such seasonal variation was found in Sciurus carolinensis.
• 5.5. Hibernation did not affect l-gulonolactone oxidase activity in Spermophilus tridecemlineatus.
• 6.6. In four species of rodents, Microtus ochrogaster, Tylomys panamensis, Octodon degus and Sigmodon hispidus, l-gulonolactone oxidase activity was not affected by the level of dietary ascorbate.

     

Action of free radical generating systems upon the biological and immunological properties of caeruloplasmin

• 1.1. Exposure of human caeruloplasmin, an acute phase protein with antioxidant properties, to a mixture of xanthine/hypoxanthine and xanthine oxidase as a source of reactive oxygen intermediates decreased its ferroxidase and ascorbate oxidase activities and its ability to inhibit lipid peroxidation.
• 2.2. Immunological reactivity was also altered.
• 3.3. Exposure to hydrogen peroxide mimicked these effects.
• 4.4. Exposure to low-intensity u.v. irradiation depressed caeruloplasmin's ability to inhibit iron-catalysed hyaluronic acid degradation.
• 5.5. The results may explain the mechanism of the observed inactivation of caeruloplasmin within human rheumatoid synovial fluid.

     

Gender-related differences of mouse liver d-aspartate oxidase in the activity and response to administration of d-aspartate and peroxisome proliferators

• 1.1. The hepatic d-aspartate oxidase activity was found to be higher in female ddY and ICR mice than in their male counterparts. On the contrary, the free d-aspartate content in the liver was lower in female mice than in male mice, suggesting that d-aspartate is actually metabolized by d-aspartate oxidase in vivo.
• 2.2. Oral administration of d-aspartate to the animals increased the hepatic d-aspartate oxidase activity 2–3 fold in both genders without any significant difference in the rate of the increase between the genders.
• 3.3. Several peroxisomal enzyme activities other than d-aspartate oxidase examined were not affected by this treatment.
• 4.4. Experiments in vitro suggested that the increase in the d-aspartate activity might be explained in part by stabilization of the enzyme by d-aspartate.
• 5.5. The administration of clofibrate, a peroxisome proliferator, to male mice, increased the hepatic d-aspartate oxidase activity with a significant simultaneous decrease of d-aspartate content in the liver, in agreement with a possible role of the enzyme n vivo.
• 6.6. On the other hand, the administration of clofibrate or dehydroepiandrosterone to female mice decreased the d-aspartate oxidase activity.
• 7.7. The peroxisome proliferators were suggested to act to eliminate the gender difference of hepatic d-aspartate oxidase activity in mice.

     

Effect of methyl methacrylate on mitochondrial function and structure

• 1.1. Treatment of isolated rat liver mitochondria with methyl methacrylate (MM) produced membrane disruption as evidenced by the release of citrate synthase, and changes in the ultrastructure of mitochondria.
• 2.2. At concentration 0.1%, MM uncoupled oxidative phosphorylation as evidenced by stimulation of state 4 respiration supported either by pyruvate plus malate or succinate (+rotenone) and ATP-ase activity in intact mitochondria.
• 3.3. At concentration 1% MM stimulated ATP-ase activity in intact mitochondria and succinate (+rotenone) oxidation at state 4 and was without effect on this substrate oxidation at state 3.
• 4.4. MM inhibited pyruvate plus malate oxidation either at state 3 or in the presence of uncoupling agents.
• 5.5. MM inhibited the NADH oxidase of electron transport particles at a concentration which failed to inhibit either succinic oxidase or the NADH-ferricyanide reductase activity.
• 6.6. The data presented suggest that in the isolated mitochondria MM inhibits NADH oxidation in the vicinity of the rotenone sensitive site of complex I.
• 7.7. The general conclusion is that MM may block an electron transport and to uncouple oxidative phosphorylation in rat liver mitochondria. The overall in vitro effect would be to prevent ATP synthesis which could result in cell death under in vivo conditions.

     

Characterization of bovine liver guanine aminohydrolase

• 1.1. The isoelectric points of bovine liver guanine aminohydrolase and xanthine oxidase are 4.90 and 6.25, respectively.
• 2.2. The molecular weight of the guanine aminohydrolase is 95,000.
• 3.3. The guanine aminohydrolase is formed from two subunits of identical molecular weight.

     

Purification and properties of glycollate oxidase from Lemna minor L.

• 1.1. Glycollate oxidase has been purified to apparent homogeneity from Lemna minor L. grown on medium containing 7mM NO⁻₃.
• 2.2. The enzyme is a highly basic protein with a sub-unit molecular weight of 42,000 and a holoprotein molecular weight of 250,000.
• 3.3. The Lemna enzyme is a flavoprotein with a broad specificity for straight chain α-hydroxy acids, the preferred substrate being glycollate.
• 4.4. It is also competitively inhibited by oxalate and phenyllactate.
• 5.5. A comparison is drawn between the physical properties of glycollate oxidase from a number of higher plants and the degree of sub-unit aggregation in the resulting protomers.

     

Patterns of hemoglobin production in the adult newt (Triturus cristatus) erythron following induction of anemia

• 1.1. Changes in the hemoglobins present in many vertebrates have been observed during development and during anemic episodes.
• 2.2. A change in the number of hemoglobins present and their relative amounts was observed when adult Triturus cristalus newts were made anemic by injection of acetylphenylhydrazine.
• 3.3. Hemoglobin IV, which is a minor hemoglobin in healthy adults, was found to be a major component during the subsequent erythropoietic response to hemolytic anemia.
• 4.4. No new hemoglobin not already present in the non-anemic state was detected during the response to induced anemia.

     

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The effect of feed restriction on certain haematological indices,enzymes and metabolites in Nubian goats

• 1.1. Some effects of restricting feed intake for 96 or 168 hr were determined in male Nubian goats.
• 2.2. Goats restricted for 96 hr lost 11.6% of their body weight, and goats restricted for 168 hr lost 19.8%.
• 3.3. Feed restriction for up to 168 hr did not produce significant effects on the heart rate, respiratory rate or rectal temperature.
• 4.4. Haemoglobin concentration, packed cell volume and erythrocyte number were all decreased by feed restriction. There was also a tendency towards eosinopenia and lymphopenia.
• 5.5. Feed restriction for 96 or 168 hr raised the plasma activity of aspartate transaminase, and did not affect significantly cholinesterase activity. Plasma amine oxidase activity was significantly reduced in goats restricted for 168 hr.
• 6.6. Feed restriction produced significant increases in the blood or plasma concentrations of lactate. pyruvate, non-esterified fatty acids, cholesterol, ketone bodies and bilirubin.
• 7.7. Significant decreases were found in the concentrations of total protein and calcium.
• 8.8. No significant changes were observed in the plasma concentrations of glucose, sodium or potassium.

     

Structural analogies between different redox enzymes inserted into biological membranes

• 1.1. We have compared the primary structure and the predicted secondary structure of subunit I (COI) of cytochrome oxidase with those of other integral redox enzymes which contain membrane-buried iron centres.
• 2.2. Some striking analogies have been found between the deduced transmembrane folding for COI and the known three-dimensional structure of the photosynthetic reaction centre of Rhodobacter sphaeroides.
• 3.3. These structural analogies are paralleled by a fundamental functional analogy between these two redox systems, since they both oxidize reduced cytochrome c at the positive side of the membrane, transferring electrons to membrane-buried metal centres.
• 4.4. A statistical evaluation has been performed on the amino acid composition of the peptides containing known histidine ligands of the membrane-buried iron in cytochrome b of the bc 1 complex and in the bacterial reaction centre.
• 5.5. This evaluation was then applied to the peptides which contain conserved histidines in subunit I of cytochrome oxidase, subunit that is known to bind both haem a and a3, indicating which of these histidines are the most likely ligands of the membrane-buried iron of the a-haems.
• 6.6. A sequence homology has been found between the known oxygen binding site and the haem binding peptide in cyt P450 and two peptides which are conserved in all the sequences of COI, thus indicatingt the possible oxygen catalytic site of cytochrome oxidase.

     

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The mechanism of interaction of ceruloplasmin with superoxide radicals

• 1.1. The mechanism of interaction of CP with O₂ radicals in chemical and enzymatic systems of Superoxide radical generation as well as in the pulse radiolysis technique was studied.
• 2.2. It is found that CP does not exert any kinetic influence on the decomposition of Superoxide radical and, unlike SOD, cannot catalyze the reaction of disproportionation of these radicals in systems with chemical and enzymatic generation of O₂⁻.
• 3.3. The data obtained confirm the suggestion that CP interacts with precursors of ₂⁻ radicals.
• 4.4. The irradiation of CP does not change its inhibiting activity in the reaction of the formation of Superoxide radicals in systems with enzymatic O₂⁻ generation, but decreases its oxidase activity.
• 5.5. The results obtained demonstrated that the increase in the radiation dose resulted in the decrease of the inhibiting activity of SOD, whereas the activity of CP did not change.

     

Prostaglandin E1 and analogs of prostacyclin influencing superoxide production by the human neutrophil nadph oxidase system

• 1.1. The effects of prostaglandin (PG) E₁, and I₂ analogs (OP-41483 and OP-2507) on the Superoxide generation of human neutrophil NADPH oxidase (EC 1.6.99.6) in both whole-cell and cell-free systems were investigated.
• 2.2. In a whole-cell system, OP-2507 inhibited the Superoxide generation by neutrophils exposed to phorbol myristate acetate concentration-dependently through its superoxide-scavenging action.
• 3.3. The concentration of the drug required for 50% inhibition of the oxidase (IC₅₀) was 21 μM.
• 4.4. In a cell-free system, however, the drug in concentrations of < 100 μM did not inhibit the activation of NADPH oxidase by sodium dodecyl sulfate because of its inactivation by the detergent.
• 5.5. Although PGE₁ and OP-41483 did not inhibit the Superoxide production by stimulated neutrophils in a whole-cell system, they both inhibited the activation of NADPH oxidase in a cell-free system concentration-dependently, with IC₅₀ values of 44 and 170 μM, respectively.
• 6.6. In addition, in the cell-free system, the K_m value for NADPH of the oxidase was unchanged by PGE₁.
• 7.7. The results suggest that the PGI₂ analog, OP-2507, is a possible superoxide-scavenger and that PGE₁ inhibits the NADPH oxidase activation by sodium dodecyl sulfate in a cell-free system concentration-dependently.

     

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Occurrence of d-alanine in the eggs and the developing embryo of the sea urchin Paracentrotus lividus

• 1.1. d-Alanine has been found in appreciable amounts in the eggs and embryos of the sea urchin Paracentrotus lividus.
• 2.2. The content of d-alanine, expressed as pmol/egg or embryo, is 1.32 in the egg, 0.81 in the blastula, 0.54 in the gastrula and 0.60 in the pluteus.
• 3.3. The percentage of d-alanine with respect to the total alanine (d + l) decreases during embryonic development.
• 4.4. d-Amino acid oxidase, d-alanine transaminase and d-alanine racemase activities were found neither in eggs nor in embryos.
• 5.5. Therefore, it does not appear likely that d-alanine is subject to oxidative metabolism.
• 6.6. The decrease in this d-amino acid during development may be due to its utilization in the synthesis of a more complex molecule.

     

On the synthesis and incorporation of catalase and urate oxidase into the peroxisomes of mouse liver

• 1.1. The processes associated with the biogenesis of peroxisomes in mouse liver have been studied by following the incorporation of radiolabelled leucine into major enzymic components of this organelle.
• 2.2. Maximal incorporation of label into peroxisomal catalase and urate oxidase occurred within 2 hr, with the urate oxidase being labelled before catalase, but subsequent to the incorporation of phospholipid into this organelle.
• 3.3. Subsequently, immunoprecipitation of catalase from the large granular fraction of mouse liver was shown to result in the isolation of a catalase molecule which had lost a peptide of approx. 2000 dalton from each subunit by comparison with the newly-synthesized enzyme.
• 4.4. It was observed that the modification of catalase was obviated by the presence of leupeptin and iodoacetamide and this information has enabled the purification of both modified and unmodified forms of the enzyme.
• 5.5. The possible significance of these data has been discussed and the major features incorporated into a working model of peroxisomal biogenesis.

     

Isolation and characterization of phospholipase A2, from Agkistrodon bilineatus (common cantil) venom

• 1.1. Phospholipase A₂ was isolated from Agkistrodon bilineatus venom by Sephadex G-75 and CM-Cellulose column chromatographies.
• 2.2. The purified phospholipase A₂-I gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoresis.
• 3.3. The enzyme preparation had a molecular weight of 14,000, isoelectric point of pH 8.77 and possessed 123 amino acid residues.
• 4.4. The purified phospholipase A₂ possessed lethal, indirect hemolytic and anticoagulant activities.
• 5.5. The enzyme hydrolyzed the phospholipids phosphatidyl choline (PC), phosphatidyl ethanolamine (PE), phosphatidyl inositol (PI) and phosphatidyl serine (PS).
• 6.6. The concentration of mouse diaphragm was inhibited and the contraction of guinea pig left atrium was increased by phospholipase A₂-I.
• 7.7. Phospholipase A₂ activity of this preparation was inhibited by ethylenediamine tetraacetic acid, p-bromo phenacyl bromide, n-bromo succinimide or dithiothreitol, but not by diisopropyl fluorophosphate or benzamidine.